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Protein Page:
Daxx (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
Daxx a transcriptional co-regulatory protein. Proposed to mediate activation of the JNK pathway and apoptosis via ASK1 in response to signaling from FAS and TGF-betaR2. Glucose deprivation activates the ASK1-SEK1-JNK1-HIPK1 pathway, relocalizing Daxx from the nucleus to the cytoplasm, where Daxx binds to ASK1, and subsequently leads to ASK1 oligomerization. Interaction with HSP27 may prevent interaction with TGF-betaR2 and ASK1 and block DAXX-mediated apoptosis. Seems to act as a transcriptional co- repressor and inhibits PAX3 and ETS1 through direct protein- protein interaction. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Two alternatively spliced isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: Apoptosis; Transcription, coactivator/corepressor; Nuclear receptor co-regulator
Cellular Component: heterochromatin; PML body; neuron projection; cytoplasm; nucleolus; cell cortex; nucleus; cytosol; chromosome, pericentric region
Molecular Function: protein binding; protein homodimerization activity; enzyme binding; androgen receptor binding; p53 binding; heat shock protein binding; ubiquitin protein ligase binding; receptor signaling protein activity; protein N-terminus binding; transcription factor binding
Biological Process: cytokinesis after mitosis; transcription, DNA-dependent; induction of apoptosis via death domain receptors; regulation of transcription, DNA-dependent; regulation of protein ubiquitination; apoptosis; virus-host interaction; androgen receptor signaling pathway; induction of apoptosis; negative regulation of transcription, DNA-dependent; activation of JNK activity
Reference #:  Q9UER7 (UniProtKB)
Alt. Names/Synonyms: BING2; CENP-C binding protein; DAP6; DAXX; Death domain-associated protein 6; death-associated protein 6; death-domain associated protein; EAP1; ETS1-associated protein 1; Fas death domain-associated protein; Fas-binding protein; hDaxx; MGC126245; MGC126246
Gene Symbols: DAXX
Molecular weight: 81,373 Da
Basal Isoelectric point: 4.8  Predict pI for various phosphorylation states
CST Pathways:  Death Receptor Signaling  |  SAPK/JNK Signaling Cascades  |  Signaling Pathways Activating p38 MAPK
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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Daxx
Protein Structure Not Found.


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Sites Implicated In
apoptosis, altered: S737‑p, S739‑p
apoptosis, induced: S176‑p, S184‑p
apoptosis, inhibited: S178‑p
transcription, altered: S737‑p, S739‑p
intracellular localization: S668‑p
molecular association, regulation: S178‑p, S668‑p, S737‑p, S739‑p
protein degradation: S178‑p
protein stabilization: S176‑p, S184‑p
sumoylation: S737‑p, S739‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


  MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


        human

 
1 0 K122-u RARSRPAkLyVyINE
0 5 Y124-p RSRPAkLyVyINELC
0 5 Y126-p RPAkLyVyINELCTV
2 0 S176-p TNAENTAsQsPRTRG
1 8 S178-p AENTAsQsPRTRGsR
2 0 S184-p QsPRTRGsRRQIQRL
0 1 K208-u EIRRLQEkELDLsEL
0 6 S213-p QEkELDLsELDDPDS
0 1 K243 FGRLCELKDCsSLtG
0 1 S246-p LCELKDCsSLtGRVI
0 1 T249-p LKDCsSLtGRVIEQR
0 1 K277-u RIERLINkPGPDTFP
0 1 Y334-p RRHLDLIyNFGCHLT
0 2 Y344-p GCHLTDDyRPGVDPA
0 2 K378-u RLDEVISkyAMLQDk
0 1 Y379-p LDEVISkyAMLQDkS
0 1 K385-u kyAMLQDkSEEGERK
0 4 T408-p TSSHSADtPEAsLDs
0 3 S412-p SADtPEAsLDsGEGP
0 3 S415-p tPEAsLDsGEGPsGM
0 1 S420-p LDsGEGPsGMAsQGC
0 15 S424-p EGPsGMAsQGCPSAS
0 1 T459 EEEEEEATDSEEEED
1 53 S495-p AGKDGDKsPMsSLQI
0 3 S498-p DGDKsPMsSLQISNE
1 6 L508 QISNEKNLEPGkQIs
0 1 K512-a EKNLEPGkQIsRSSG
0 1 K512-u EKNLEPGkQIsRSSG
0 1 S515-p LEPGkQIsRSSGEQQ
0 9 S517 PGkQIsRSSGEQQNK
0 1 S529 QNKGRIVSPSLLSEE
0 1 L532 GRIVSPSLLSEEPLA
1 0 S564-p LEEESPVsQLFELEI
0 1 G626 PHNWGDSGPPCkkSR
4 0 K630-s GDSGPPCkkSRKEKK
4 0 K631-s DSGPPCkkSRKEKKQ
0 1 Y648-p SGPLGNSyVERQRsV
0 11 S654-p SyVERQRsVHEKNGK
0 1 T665-p KNGKKICtLPsPPsP
4 5 S668-p KKICtLPsPPsPLAs
1 2 P670 ICtLPsPPsPLAsLA
0 12 S671-p CtLPsPPsPLAsLAP
0 2 S675-p sPPsPLAsLAPVADS
0 10 S688-p DSSTRVDsPsHGLVt
0 4 S690-p STRVDsPsHGLVtSS
0 2 T695-p sPsHGLVtSSLCIPs
0 11 S702-p tSSLCIPsPARLsQt
0 1 S707-p IPsPARLsQtPHsQP
0 2 T709-p sPARLsQtPHsQPPR
0 1 S712-p RLsQtPHsQPPRPGT
1 11 S737-p PEEIIVLsDsD____
1 11 S739-p EIIVLsDsD______
  mouse

 
K128 RSRKRPAKIYVYINE
Y130 RKRPAKIYVYINELC
Y132 RPAKIYVYINELCTV
S182 TNTENTASEASRTRG
A184 TENTASEASRTRGSR
S190 EASRTRGSRRQIQRL
K214 EIRRLQEKELDLsEL
S219-p QEKELDLsELDDPDS
K249-u FGRLCELkDCSSLTG
S252 LCELkDCSSLTGRVI
T255 LkDCSSLTGRVIEQR
K283 RIERLINKPGLDTFP
Y340 RRHLDLIYNFGCHLT
Y350 GCHLTDDYRPGVDPA
K384 RLDEVISKYAMMQDK
Y385 LDEVISKYAMMQDKT
K391 KYAMMQDKTEEGERQ
P414 TAPQPSDPPQASSES
S418 PSDPPQASSESGEGP
S421 PPQASSESGEGPSGM
S426 SESGEGPSGMASQEC
S430 EGPSGMASQECPTTS
T472-p EEEEKEAtEDEDEDL
S502-p GDNEGNEsPTSPSDF
S505 EGNEsPTSPSDFFHR
S515-p DFFHRRNsEPAEGLR
E519 RRNsEPAEGLRtPEG
E519 RRNsEPAEGLRtPEG
L521 NsEPAEGLRtPEGQQ
T523-p EPAEGLRtPEGQQKR
T535-p QKRGLTEtPAsPPGA
S538-p GLTEtPAsPPGASLD
S570 LGDESPVSQLAELEM
S626-p SHTWRDAsPPSKRFR
K630 RDAsPPSKRFRKEKK
R631 DAsPPSKRFRKEKKQ
Y648 SGLLGNSYIKEPMAQ
- gap
- gap
M667 QNTSVQPMPsPPLAS
S669-p TSVQPMPsPPLASVA
P670 SVQPMPsPPLASVAS
S674 MPsPPLASVASVADS
S687-p DSSTRVDsPsHELVt
S689-p STRVDsPsHELVtSS
T694-p sPsHELVtSSLCSPs
S701-p tSSLCSPsPSLLLQT
- gap
T708 sPSLLLQTPQAQSLR
A711 LLLQTPQAQSLRQCI
S736-p PEEIIVLsDsD____
S738-p EIIVLsDsD______
  rat

 
K122 RSRNRPAKLYVYINE
Y124 RNRPAKLYVYINELC
Y126 RPAKLYVYINELCTV
S174 TNTETTASEASRTRG
A176 TETTASEASRTRGSR
S182 EASRTRGSRRQIQRL
K206 EIQRLQEKELDLSEL
S211 QEKELDLSELDDPDS
K241 FGRLCDLKDCSSLTG
S244 LCDLKDCSSLTGKVI
T247 LKDCSSLTGKVIEQR
K275 RIERLINKPGPDTFP
Y332 RRHLDLIYNFGCHLT
Y342 GCHLTDDYRPGVDPA
K376 RLDEVISKYAMMQDK
Y377 LDEVISKYAMMQDKS
K383 KYAMMQDKSEEGERQ
L405 ATSQSSDLPKASSDS
S409 SSDLPKASSDSGEGP
S412 LPKASSDSGEGPSGV
S417 SDSGEGPSGVASQED
S421 EGPSGVASQEDPTTP
T456 EEEEEEATEDEDEDL
S485 GDNEDDKSPASPSPI
S488 EDDKSPASPSPIFRR
S499 IFRRKEFSNPQKGSG
K503 KEFSNPQKGSGPQEE
K503 KEFSNPQKGSGPQEE
S505 FSNPQKGSGPQEEQQ
P507 NPQKGSGPQEEQQER
T519 QERGLTGTPASPLEA
S522 GLTGTPASPLEASPG
S554 LAGESPVSQLSELDM
S617 SHPCRDASPPSKRFR
K621 RDASPPSKRFRKEKK
R622 DASPPSKRFRKEKKQ
Y639 PGPLGNSYVKKQTMA
- gap
- gap
T659 WKISVLSTPssPLAS
S661-p ISVLSTPssPLASVG
S662-p SVLSTPssPLASVGP
S666 TPssPLASVGPVADS
S679 DSSTRVDSPSHELVT
S681 STRVDSPSHELVTSS
T686 SPSHELVTSSLCNPS
S693 TSSLCNPSPSLILQT
- gap
T700 SPSLILQTPQSQSPR
S703 LILQTPQSQSPRPCI
S728 PEEIIVLSDSD____
S730 EIIVLSDSD______
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